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Q5WGA4 (PANC_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate synthetase

Short name=PS
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene names
Name:panC
Ordered Locus Names:ABC2066
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP-Rule MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128201

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1761ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WGA4 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 05A1477DEAB1AADB

FASTA30233,279
        10         20         30         40         50         60 
MIEVQTTSQL QEQLQDAREQ GKTIGFVPTM GALHGGHQSL VRACAQTCDL VVVSIYVNPL 

        70         80         90        100        110        120 
QFGPHEDYHE YPRQLEKDRV LAEEAGCDVL FCPTDEEIYP DGYTQTVHVK QGANVLCGKS 

       130        140        150        160        170        180 
RPGHFDGVAT VVLKLFMLVQ PDFAFFGEKD AQQVAIIKQL VKEFFLPVTI VACPTVREDD 

       190        200        210        220        230        240 
GLAKSSRNAN LTPAERQVAP KLYAALRDAA KSPTSQLSDL VQQVRQHLAA LPLGCIDYVE 

       250        260        270        280        290        300 
AYEYPSLKKV EQSDGIVILA LAYQFSKARL IDHILIDMNN RNGGLNDVSD NDESKIASCT 


GD 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD64601.1.
RefSeqYP_175562.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WGA4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC2066.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD64601; BAD64601; ABC2066.
GeneID3202072.
KEGGbcl:ABC2066.
PATRIC18923676. VBIBacCla58185_2201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAFFGMKDA.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-2134-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_BACSK
AccessionPrimary (citable) accession number: Q5WGA4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways